{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Seo T"],"funding":["National Research Council of Science and Technology","Ministry of Science, ICT and Future Planning","National Research Foundation of Korea","Korea Research Institute of Bioscience and Biotechnology"],"pagination":["3725-3741"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8038991"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["78(7)"],"pubmed_abstract":["Protein arginylation is a critical regulator of a variety of biological processes. The ability to uncover the global arginylation pattern and its associated signaling pathways would enable us to identify novel disease targets. Here, we report the development of a tool able to capture the N-terminal arginylome. This tool, termed R-catcher, is based on the ZZ domain of p62, which was previously shown to bind N-terminally arginylated proteins. Mutating the ZZ domain enhanced its binding specificity and affinity for Nt-Arg. R-catcher pulldown coupled to LC-MS/MS led to the identification of 59 known and putative arginylated proteins. Among these were a subgroup of novel ATE1-dependent arginylated ER proteins that are linked to diverse biological pathways, including cellular senescence and vesi"],"journal":["Cellular and molecular life sciences : CMLS"],"pubmed_title":["R-catcher, a potent molecular tool to unveil the arginylome."],"pmcid":["PMC8038991"],"funding_grant_id":["2020R1A2C2003685","CAP-16-03-LROBB","2020R1A2C1010512"],"pubmed_authors":["Cha-Molstad H","Kim J","Hwang J","Seo T","Nawale L","Lee C","Lee HS","Soung NK","Bang G","Kim JY","Shin HC","Bang JK","Han G","Kim JG","Ju S","Kim SJ","Kim BY","Lee KH"],"additional_accession":[]},"is_claimable":false,"name":"R-catcher, a potent molecular tool to unveil the arginylome.","description":"Protein arginylation is a critical regulator of a variety of biological processes. The ability to uncover the global arginylation pattern and its associated signaling pathways would enable us to identify novel disease targets. Here, we report the development of a tool able to capture the N-terminal arginylome. This tool, termed R-catcher, is based on the ZZ domain of p62, which was previously shown to bind N-terminally arginylated proteins. Mutating the ZZ domain enhanced its binding specificity and affinity for Nt-Arg. R-catcher pulldown coupled to LC-MS/MS led to the identification of 59 known and putative arginylated proteins. Among these were a subgroup of novel ATE1-dependent arginylated ER proteins that are linked to diverse biological pathways, including cellular senescence and vesi","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-02T10:48:59.376Z","creation":"2022-02-09T08:02:08.9Z"},"accession":"S-EPMC8038991","cross_references":{"pubmed":["33687501"],"doi":["10.1007/s00018-021-03805-x"]}}